7PC1
DNA binding domain of partition protein StbA of plasmid R388
Summary for 7PC1
| Entry DOI | 10.2210/pdb7pc1/pdb |
| Descriptor | StbA (2 entities in total) |
| Functional Keywords | plasmid conjugation, plasmid partition, helix-turn-helix, dna binding protein |
| Biological source | Escherichia coli K-12 |
| Total number of polymer chains | 1 |
| Total formula weight | 8600.47 |
| Authors | Guynet, C.,Moncalian, G. (deposition date: 2021-08-03, release date: 2022-08-10, Last modification date: 2024-11-13) |
| Primary citation | Quebre, V.,Del Campo, I.,Cuevas, A.,Siguier, P.,Rech, J.,Le, P.T.N.,Ton-Hoang, B.,Cornet, F.,Bouet, J.Y.,Moncalian, G.,de la Cruz, F.,Guynet, C. Characterization of the DNA Binding Domain of StbA, A Key Protein of A New Type of DNA Segregation System. J.Mol.Biol., 434:167752-167752, 2022 Cited by PubMed Abstract: Low-copy-number plasmids require sophisticated genetic devices to achieve efficient segregation of plasmid copies during cell division. Plasmid R388 uses a unique segregation mechanism, based on StbA, a small multifunctional protein. StbA is the key protein in a segregation system not involving a plasmid-encoded NTPase partner, it regulates the expression of several plasmid operons, and it is the main regulator of plasmid conjugation. The mechanisms by which StbA, together with the centromere-like sequence stbS, achieves segregation, is largely uncharacterized. To better understand the molecular basis of R388 segregation, we determined the crystal structure of the conserved N-terminal domain of StbA to 1.9 Å resolution. It folds into an HTH DNA-binding domain, structurally related to that of the PadR subfamily II of transcriptional regulators. StbA is organized in two domains. Its N-terminal domain carries the specific stbS DNA binding activity. A truncated version of StbA, deleted of its C-terminal domain, displays only partial activities in vivo, indicating that the non-conserved C-terminal domain is required for efficient segregation and subcellular plasmid positioning. The structure of StbA DNA-binding domain also provides some insight into how StbA monomers cooperate to repress transcription by binding to the stbDR and to form the segregation complex with stbS. PubMed: 35868361DOI: 10.1016/j.jmb.2022.167752 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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